Purification and Properties of a Monofunctional Imidazoleglycerol-Phosphate Dehydratase from Wheat.

@article{Mano1993PurificationAP,
  title={Purification and Properties of a Monofunctional Imidazoleglycerol-Phosphate Dehydratase from Wheat.},
  author={Ji. Mano and Maki Hatano and Si. Koizumi and Sachiyo Tada and Mitsuru Hashimoto and Alfred Scheidegger},
  journal={Plant physiology},
  year={1993},
  volume={103 3},
  pages={733-739}
}
Imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) activity was detected in extracts of several monocotyledonous and dicotyledonous plants using a newly developed assay method. The enzyme was purified 114,000-fold (to apparent homogeneity) from wheat germ by five chromatographic steps. Its native relative molecular weight (Mr) was determined to be 600,000 to 670,000, and it consists of identical subunits of Mr 25,500. In wheat germ, the dehydratase, unlike those of prokaryotic origin, is not… CONTINUE READING